Protein kinases are an important class of substrate of the protein phosphatases. We have examined the mechanism of dephosphorylation of the activation segments of the insulin receptor kinase and cyclin-dependent kinase 2 by their respective phosphatases, namely the tyrosine specific phosphatase PTP1B and the dual specificity phosphatase KAP. These studies reveal that PTP1B and KAP utilize contrasting mechanisms in order to dephosphorylate their substrates specifically.
Keywords:
dual specificity protein phosphatases (DSPs),
insulin receptor,
insulin receptor kinase (IRK),
kinase-associated phosphatase (KAP),
phosphoproteins,
protein tyrosine phosphatase IB (PTPIB),
PTP, protein tyrosine phosphatase,
DSP, dual specificity protein phosphatase,
IR(K), insulin receptor (kinase),
KAP, kinase-associated phosphatase
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© 2001 Biochemical Society
2001
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